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Interaction of two botulinum subdomains needed to elicit antibodies.

Vaccine Weekly

| November 03, 2004 | COPYRIGHT 2004 NewsRX. This material is published under license from the publisher through the Gale Group, Farmington Hills, Michigan.  All inquiries regarding rights should be directed to the Gale Group. (Hide copyright information)Copyright

2004 NOV 3 - (NewsRx.com & NewsRx.net) -- Interaction between the two subdomains of the C-terminal part of the botulinum neurotoxin A is essential for the generation of protective antibodies.

According to a study from France, "The botulinum neurotoxin A C-terminal fragment (He), which mediates the binding of the toxin to neuronal cell surface receptors, comprises two subdomains, Hc-N (amino acids 873-1095) and Hc-C (amino acids 1096-1296). In order to define the minimal fragment of He carrying protective antigenic properties, He, Hc-N and Hc-C have been produced as recombinant proteins in Escherichia coli, and have been tested for their antigenicity in mouse protection assays. He, Hc-N, and Hc-C induced similar antibody levels as shown by ELISA."

"However, a single immunization with He (10 microgram) fully protected mice challenged with 10[superscript]3 mouse lethal dose 50 of toxin, whereas Hc-N, Hc-C, or Hc-N plus Hc-C did not give any protection," reported Mahmood Tavallaie at the Institute Pasteur in Paris and collaborators in France. "Triple immunizations with Hc-N or Hc-C were necessary to induce a higher level of protection. Circular dichroism and fluorescence studies showed that the isolated subdomains were folded and stable. However, an intense near-UV dichroic signal ...

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Source: HighBeam Research, Interaction of two botulinum subdomains needed to elicit antibodies.

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